Biochemistry of copper site assembly in heme-copper oxidases: a theme with variations
Copper is an essential cofactor for aerobic respiration, since it is required as a redox cofactor in Cytochrome c Oxidase (COX). This ancient and highly conserved enzymatic complex from the family of heme-copper oxidase possesses two copper sites: CuA and CuB. Biosynthesis of the oxidase is a com...
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| Autores principales: | , , |
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| Formato: | article artículo publishedVersion |
| Lenguaje: | Inglés |
| Publicado: |
MDPI
2021
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/2133/20012 http://hdl.handle.net/2133/20012 |
| Aporte de: |
| Sumario: | Copper is an essential cofactor for aerobic respiration, since it is required as a redox cofactor
in Cytochrome c Oxidase (COX). This ancient and highly conserved enzymatic complex from the
family of heme-copper oxidase possesses two copper sites: CuA and CuB. Biosynthesis of the oxidase
is a complex, stepwise process that requires a high number of assembly factors. In this review, we
summarize the state-of-the-art in the assembly of COX, with special emphasis in the assembly of
copper sites. Assembly of the CuA site is better understood, being at the same time highly variable
among organisms. We also discuss the current challenges that prevent the full comprehension of the
mechanisms of assembly and the pending issues in the field. |
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